Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

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Models for biomedical interfaces: a computational study of quinone-functionalized amorphous silica surface features.

P2860

Q48162111-6A33EE9E-2CDB-4B52-A3CF-052FF36F9F24

P2860

Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

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http://www.wikidata.org/entity/Q41892966

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1995 nî lūn-bûn

@nan

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

1995年论文

@zh

1995年论文

@zh-cn

name

Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

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type

Item

label

Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

@en

prefLabel

Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

@en

P1476

Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

@en

P2093

L H Jones

http://www.w3.org/2001/XMLSchema#string

M E Graichen

http://www.w3.org/2001/XMLSchema#string

V L Davidson

http://www.w3.org/2001/XMLSchema#string

P2860

Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine

Microbial oxidation of amines. Spectral and kinetic properties of the primary amine dehydrogenase of Pseudomonas AM1

Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor

Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data.

Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center.

Quinoenzymes in biology.

Steady-state kinetic analysis of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans.

Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins.

Redox properties of the quinoprotein methylamine dehydrogenase from paracoccus denitrificans.

A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase.

P304

487-492

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P31

scholarly article

P356

10.1042/BJ3080487

http://www.w3.org/2001/XMLSchema#string

P407

English

P478

308 ( Pt 2)

http://www.w3.org/2001/XMLSchema#string

P577

1995-06-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

15427224

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P698

7772031

http://www.w3.org/2001/XMLSchema#string

P932

1136951

http://www.w3.org/2001/XMLSchema#string

Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

about

P2860

P2860

Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P478

P577

P5875

P698

P932